Review
doi: 10.1248/yakushi1947.105.5_430.
[Development of "inverse substrates" for trypsin. Application to the studies on the structure and function of the enzyme and to the design for biologically active compounds]
[Article in
Japanese]
- PMID: 3162015
- DOI: 10.1248/yakushi1947.105.5_430
Item in Clipboard
Review
[Development of "inverse substrates" for trypsin. Application to the studies on the structure and function of the enzyme and to the design for biologically active compounds]
[Article in
Japanese]
Yakugaku Zasshi.
1985 May.
No abstract available
Similar articles
-
Enantiomeric specificity at the deacylation process of tryptic catalysis.Biochim Biophys Acta. 1987 Nov 26;916(2):205-12. doi: 10.1016/0167-4838(87)90110-5. Biochim Biophys Acta. 1987. PMID: 3676332
-
Behavior of trypsin and related enzymes toward amidinophenyl esters.J Pharmacobiodyn. 1981 Aug;4(8):559-64. doi: 10.1248/bpb1978.4.559. J Pharmacobiodyn. 1981. PMID: 6457906
-
Oxygen and sulfur esters of "inverse substrates": different responses of amidinophenol and amidinothiophenol in the activation of the rate of tryptic hydrolysis of the inverse esters.J Biochem. 1985 Jan;97(1):275-80. doi: 10.1093/oxfordjournals.jbchem.a135051. J Biochem. 1985. PMID: 3997793
-
Trypsin: a case study in the structural determinants of enzyme specificity.Biol Chem. 1996 Jul-Aug;377(7-8):465-70. Biol Chem. 1996. PMID: 8922280 Review.
-
Nonconventional amide bond formation catalysis: programming enzyme specificity with substrate mimetics.Braz J Med Biol Res. 2000 May;33(5):469-85. doi: 10.1590/s0100-879x2000000500001. Braz J Med Biol Res. 2000. PMID: 10775878 Review.